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Ubiquitin-conjugating enzyme E2C: a potential cancer biomarker.

Abstract

The ubiquitin-conjugating enzymes 2C (UBE2C) is an integral component of the ubiquitin proteasome
system. UBE2C consists of a conserved core domain containing the catalytic Cys residue and an N-terminal extension. The core domain is required for ubiquitin adduct formation by interacting with the ubiquitinfold domain in the E1 enzyme, and contributes to the E3 enzyme binding. UBE2C N-terminal extension regulates E3 enzyme activity as a part of an intrinsic inhibitory mechanism. UBE2C is required for the destruction of mitotic cyclins and securin, which are essential for spindle assembly checkpoint and mitotic exit. The UBE2C mRNA and/or protein levels are aberrantly increased in many cancer types with poor clinical outcomes. Accumulation of UBE2C stimulates cell proliferation and anchorage-independent growth.
UBE2C transgenic mice are prone to develop spontaneous tumors and carcinogen-induced tumor with
evidence of chromosome aneuploidy.